ArticleJournal of the American Society for Mass Spectrometry2017
Subcritical Water Hydrolysis of Peptides: Amino Acid Side-Chain Modifications.
Article in Journal of the American Society for Mass Spectrometry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed.
- Defatted chia (Current research in food science · 2025Review
- Local and Systemic Peptide Therapies for Soft Tissue Regeneration: A Narrative Review.The Yale journal of biology and medicine · 2024Review
- Review
- Conventional andFood chemistry: X · 2022Article
- Protein Hydrolysis by Subcritical Water: A New Perspective on Obtaining Bioactive Peptides.Molecules (Basel, Switzerland) · 2021Review
- Fast protein analysis enabled by high-temperature hydrolysis.Chemical science · 2020Article
- Hydrolyzed Collagen-Sources and Applications.Molecules (Basel, Switzerland) · 2019Review
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Previously we have shown that subcritical water may be used as an alternative to enzymatic digestion in the proteolysis of proteins for bottom-up proteomics. Subcritical water hydrolysis of proteins was shown to result in protein sequence coverages greater than or equal to that obtained following digestion with trypsin; however, the percentage of peptide spectral matches for the samples treated with trypsin were consistently greater than for those treated with subcritical water. This observation suggests that in addition to cleavage of the peptide bond, subcritical water treatment results in other hydrolysis products, possibly due to modifications of amino acid side chains. Here, a model peptide comprising all common amino acid residues (VQSIKCADFLHYMENPTWGR) and two further model peptides (VCFQYMDRGDR and VQSIKADFLHYENPTWGR) were treated with subcritical water with the aim of probing any induced amino acid side-chain modifications. The hydrolysis products were analyzed by direct infusion electrospray tandem mass spectrometry, either collision-induced dissociation or electron transfer dissociation, and liquid chromatography collision-induced dissociation tandem mass spectrometry. The results show preferential oxidation of cysteine to sulfinic and sulfonic acid, and oxidation of methionine. In the absence of cysteine and methionine, oxidation of tryptophan was observed. In addition, water loss from aspartic acid and C-terminal amidation were observed in harsher subcritical water conditions. Graphical Abstract ᅟ.
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